Which of the following statements is TRUE regarding the Michaelis-Menten kinetics parameters in competitive inhibition? A....
An enzyme follows Michaelis-Menten kinetics. Indicate (with an "x") which of the kinetic parameters would be altered in the presence of the corresponding type of inhibitors. Inhibitor type Vmax Km Neither Both Competitive Uncompetitive Noncompetitive
Which of the following is TRUE of reactions that follow Michaelis-Menten kinetics? At both low and high substrate concentrations, rate is only dependent on total enzyme concentration. At high substrate concentrations, rate is only dependent on total enzyme concentration. At low concentrations of substrate, rate is only dependent on Vmax At both low and high substrate concentrations, rate is only dependent on substrate concentration. At low concentrations of substrate, rate is only dependent on kcat.
A single-substrate enzyme that obeys Michaelis-Menten kinetics displays the following parameters: Kd = 3.1 x 10^-5 M; k1 = 107 M-1 s-1, and kcat = 10^4 s-1. Given this information, what is the value of the Michaelis constant Km? Express your answer in terms of mM to four significant figures.
Determine the type of inhibition that has occurred in a first order Michaelis-Menten enzyme catalyzed reaction that has yielded the following data. Vi is the velocity in the presence of inhibitor, V is the velocity when run without inhibitor and [S] refers to the substrate concentration. [S] V Vi 5.00 0.29 0.16 1.25 0.27 0.15 0.45 0.23 0.13 0.22 0.19 0.10 0.13 0.14 O.08 Uncompetitive No inhibition at all O None the above ONon-competitive O Competitive Determine the type of...
4. Basic concepts of Michaelis-Menten kinetics. The Michaelis-Menten equation is expression of the relationship between the initial velocity, Vo, of an enzymatic reaction and substrate concentration, [S]. There are three conditions that are useful for simplifying the Michaelis-Menten equation: [S] <<Km; [S] = Km; [S] >> Km. Match each condition with the statement(s) that describe it. TV, Vmox[S] Vo =Vmax m . V Vo - Vmax [S] Km +[S] V. (um/min) max [S] (mm) (a) Doubling [S] will almost double...
Use the Michaelis-Menten Plot to answer question 11. If V max for the black curve is 1, what is Km? Which graph (A, B, C, or D) represent a competitive inhibition? Determine Km for your answer in b. How does competitive inhibition affect Vmax and Km?
c. 0.6 sec d. 1.67 sec 16. Which of the following about Michaelis-Menten enzyme kinetics is CORRECT? a. It assumes that the maximum reaction rate is proportional to the catalytic constant multiplied by the total enzyme concentration. b. It assumes that the enzyme-substrate complex concentration remains steady state. c. KM is defined as the substrate concentration at which the velocity of the reaction is maximal, so the unit is M. d. The KM is assigned to each enzyme regardless of...
In kinetics experiments, the hydrolysis of the substrate sialic acid by neuraminidase appears to obey Michaelis–Menten kinetics. Neuraminidase activity is critical for viral infectivity; thus, this enzyme is the target of much work by pharmaceutical companies to develop a drug to treat influenza virus infection. The drug “Tamiflu” is a competitive inhibitor of neuraminidase. Initial rate data collected at pH=6.15, 37 ∘C with 0.021 μM neuraminidase and 25.0 μM sialic acid gives a Lineweaver–Burk plot with a slope of 51.2...
The kinetics of enzyme catalyzed reactions can be described the Michaelis-Menten equation and the Eadie-Hofstee equation as shown below: V0 = (-Km) V0 / [S] + Vmax a). Please derive the Eadie-Hofstee equation starting from the Michaelis-Menten equation. b). The Vmax and Km of the enzyme catalyzed reaction can be derived from a plot of V0 versus V0/[S]. Please draw one of these plots and explain how do you use it to derive Vmax and Km. c). Please draw a...
7. a) In an enzyme catalyzed reaction which follows the Michaelis-Menten kinetics. The substrate concentration (Km, Michaelis constant) needed to reach 50% of the maximum reaction velocity (Vmax) is 20 μΜ. What substrate concentration is required to obtain at least 75% of the maximum reaction velocity? Show the work to get full points. (5 points) b) You want to load 10 μg of protein in 15 μL into one of the 10% polyacrylamide gel well. The protein needs to be...